Location of the creatine phosphokinase binding site of myosin

Houk, T. William; Putnam, Susan

doi:10.1016/s0006-291x(73)80031-2

Cited by 26 publications

(6 citation statements)

References 9 publications

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“…This identification of MM-CK with the M-bridges of the Knappeis-Carlsen model was adopted as an important feature of our recently proposed model of the M-line (64,66), in which we attempted to integrate the biochemical and ultrastructural data then available. Since it has been shown that MM-CK can bind directly to myosin molecules (5,27) as well as to myosin filaments (shown by Morimoto and Harrington [46]), at least one important criterion required of the M-bridges is fulfilled by MM-CK. Recently, it has been reported that MM-CK binds more strongly to heavy meromyosin and to myosin subfragment S-1 than it does to light meromyosin (5).…”

Section: Discussionmentioning

confidence: 99%

Localization of creatine kinase isoenzymes in myofibrils. I. Chicken skeletal muscle.

Wallimann¹,

Turner²,

Eppenberger³

1977

The Journal of Cell Biology

185

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Purified, repeatedly washed, skeletal muscle myofibrils contain approx. 0.2 U of creatine kinase (CK) activity (equivalent to 2.5 micrograms CK) per milligram dry weight; this firmly bound CK activity is estimated to represent 3-5% of the total cellular CK. It had been shown previously that the myofibrillar CK, which can be quantitatively extracted at low ionic strength and purified to homogeneity, is very similar, if not identical, to the bulk MM-CK. It is shown that the two protein preparations also have the same peptide pattern after cyanogen bromide fractionation and very similar specific activities, confirming their identity. The earlier demonstration that the bound CK is specifically located at the M-lines of isolated myofibrils has been confirmed by immunofluorescence. Antibodies directed against purified MM- and BB-CK were used in the indirect fluorescent antibody technique to study the specificity of myofibril binding sites for different forms of CK. With myofibrils from adult muscle, which has only MM-CK, as well as from early developmental stages in which BB-CK is the predominant isoenzyme, M-type CK was localized exclusively at the M-line, while greater or lesser amounts of B-type CK were found at the Z-line. The data provide strong evidence that the MM-CK at the M-lines in skeletal myofibrils is not adventitiously bound but is rather an integral element in the M-line structure. The amount of CK bound is reasonably consistent with the earlier proposal that the CK molecules might be the transverse M-bridges and appears to be sufficient to regenerate all of the ATP hydrolyzed during muscle contraction.

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Section: Discussionmentioning

confidence: 99%

Localization of creatine kinase isoenzymes in myofibrils. I. Chicken skeletal muscle.

Wallimann¹,

Turner²,

Eppenberger³

1977

The Journal of Cell Biology

185

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“…Actin concentrations were determined by measuring absorbance at 290 nm using an extinction coefficient of 2.65 × 10 4 M −1 cm −1 49. Actin monomers with bound Mg-εATP were prepared by exchanging bound Ca 2+ for Mg 2+ with the addition of 0.2 mM EGTA and 80 μM MgCl 2, removing free ATP with Dowex AGX-1 slurry (9% v/v), pelleting Dowex beads by centrifugation (14 kg for 20 s) and mixing supernatant with 200 μM εATP 42,50…”

Section: Methodsmentioning

confidence: 99%

Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11

Kucera

Koblansky

Saunders

et al. 2010

Journal of Molecular Biology

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Profilins promote actin polymerization by exchanging ADP for ATP on monomeric actin, and delivering ATP-actin to growing filament barbed ends. Apicomplexan protozoa like Toxoplasma gondii invade host cells using an actin-dependent gliding motility. Toll-like receptor 11 (TLR11) generates an innate immune response upon sensing T. gondii profilin (TgPRF). The crystal structure of TgPRF reveals a parasite-specific surface motif consisting of an acidic loop, followed by a long β-hairpin. A series of structure-based profilin mutants show that TLR11 recognition of the acidic loop is responsible for most of the IL-12 secretion response to TgPRF in peritoneal macrophages. Deletion of both the acidic loop and the β-hairpin completely abrogates IL-12 secretion. Insertion of the T. gondii acidic loop and β-hairpin into yeast profilin is sufficient to generate TLR11-dependent signaling. Substitution of the acidic loop in TgPRF with the homologous loop from the apicomplexan parasite C. parvum does not affect TLR11-dependent IL-12 secretion, while substitution with the acidic loop from P. falciparum results in reduced but significant IL-12 secretion. We conclude that the parasite-specific motif in TgPRF is the key molecular pattern recognized by TLR11. Unlike other profilins, TgPRF slows nucleotide exchange on monomeric rabbit actin, and binds rabbit actin weakly. The putative TgPRF actin-binding surface includes the β-hairpin, and diverges widely from the actin-binding surfaces of vertebrate profilins.

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“…In addition, it has been suggested that M-band polypeptides may have a dual function as enzymes and as structural elements in the contractile apparatus (Wallimann et al, 1977). The presence of creatine kinase in the M-band in physical association with myosin ATP-ase provides a potential cyclical mechanism for rephosphorylating ADP from creatine phosphate (Ottaway, 1967;Houk and Putnam, 1973). Such a mechanism may play a crucial role in the efficiency of both cardiac and skeletal muscle contraction.…”

Section: Figure 6 Scans Of Sds-gel Electrophoresis Of Cardiac Myofibrmentioning

confidence: 99%

Postnatal development of the M-band in rat cardiac myofibrils.

Anversa¹,

Olivetti²,

Bracchi³

et al. 1981

Circulation Research

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Cardiac muscle fibers in rats at 1 and 5 days after birth showed little evidence of M-bands. An ultrastructural analysis of myofibrils failed to demonstrate dense M-band material in longitudinal sections or M-bridges in transverse sections of sarcomeres. M-bands began to increase in number after 5 days of postnatal life and were present in 60% of all sarcomeres at 11 days of age. Polypeptides with molecular weights of 190,000 (Ma) and 175,000 (Mb) were obtained by polyacrylamide-sodium dodecyl sulfate (SDS) gel electrophoresis of myofibril preparations. These two proteins were found in both 1- and 11-day-old rats and were considered to be specific components of the M-band. The densitometric analysis demonstrated that Ma and mb polypeptides increased approximately 2-fold during the interval from 1 to 11 days after birth. These structural and biochemical changes of the M-band material in myocytes appear to be related to the maturation of contractile function in the young heart.

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Location of the creatine phosphokinase binding site of myosin

Cited by 26 publications

References 9 publications

Localization of creatine kinase isoenzymes in myofibrils. I. Chicken skeletal muscle.

Localization of creatine kinase isoenzymes in myofibrils. I. Chicken skeletal muscle.

Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11

Postnatal development of the M-band in rat cardiac myofibrils.

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